LGUL_VIBPA
ID LGUL_VIBPA Reviewed; 138 AA.
AC P46235;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=gloA; OrderedLocusNames=VP2109;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-138.
RC STRAIN=BB22;
RX PubMed=8021208; DOI=10.1128/jb.176.14.4219-4225.1994;
RA McCarter L.L.;
RT "MotY, a component of the sodium-type flagellar motor.";
RL J. Bacteriol. 176:4219-4225(1994).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; BA000031; BAC60372.1; -; Genomic_DNA.
DR EMBL; U06949; AAA21576.1; -; Genomic_DNA.
DR RefSeq; NP_798488.1; NC_004603.1.
DR RefSeq; WP_005480812.1; NC_004603.1.
DR AlphaFoldDB; P46235; -.
DR SMR; P46235; -.
DR STRING; 223926.28807102; -.
DR EnsemblBacteria; BAC60372; BAC60372; BAC60372.
DR GeneID; 1189621; -.
DR KEGG; vpa:VP2109; -.
DR PATRIC; fig|223926.6.peg.2019; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_1_6; -.
DR OMA; NWGTESY; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..138
FT /note="Probable lactoylglutathione lyase"
FT /id="PRO_0000168098"
FT DOMAIN 5..129
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 125
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15034 MW; 5738D502E3CA35FC CRC64;
MSNGRILHTM LRVGDLDKSI KFYTEVMGMQ LLRTNENKEY EYTLAFVGYG DESQGAVIEL
TYNWGKTEYD LGTAFGHIAI GVDDIYATCD AIKAAGGNVT REAGPVKGGT THIAFVKDPD
GYMIELIQNK QASAGLEG